US8088403B2 - Method for preparing microcapsules by coacervation - Google Patents
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- US8088403B2 US8088403B2 US12/281,585 US28158507A US8088403B2 US 8088403 B2 US8088403 B2 US 8088403B2 US 28158507 A US28158507 A US 28158507A US 8088403 B2 US8088403 B2 US 8088403B2
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- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J13/00—Colloid chemistry, e.g. the production of colloidal materials or their solutions, not otherwise provided for; Making microcapsules or microballoons
- B01J13/02—Making microcapsules or microballoons
- B01J13/06—Making microcapsules or microballoons by phase separation
- B01J13/08—Simple coacervation, i.e. addition of highly hydrophilic material
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- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J13/00—Colloid chemistry, e.g. the production of colloidal materials or their solutions, not otherwise provided for; Making microcapsules or microballoons
- B01J13/02—Making microcapsules or microballoons
- B01J13/06—Making microcapsules or microballoons by phase separation
- B01J13/10—Complex coacervation, i.e. interaction of oppositely charged particles
Definitions
- the present invention relates to a method for preparing microcapsules by coacervation, and to the use of transglutaminase for cross-linking in complex coacervation.
- the present invention relates further to coacervation methods in which a material to be encapsulated is added to a solution comprising at least one colloid below the gelling temperature of the colloid.
- Typical steps of coacervation processes generally involve (a) emulsification of a generally hydrophobic material in a solution comprising hydrocolloids, (b) coacervation (phase separation) implying the formation of a coacervate phase (c) wall formation by aggregation of the hydrocolloid around droplets of the emulsified hydrophobic material, and, (d) wall-hardening, which is generally achieved by cross-linking the hydrocolloid forming the wall thus rendering the process irreversible and making the resulting microcapsules insoluble in water, resistant to mechanical stress and to heat exposure.
- the step of wall formation is generally driven by the surface tension difference between the coacervate phase, the water and the hydrophobic material.
- one of the hydrocolloids used in coacervation processes are selected from gellable proteins. These are easier to use and less prone to aggregation after the formation of the wall when the temperature is below the gelling temperature, if compared to non-gellable hydrocolloids.
- Gellification in turn, is generally brought about by lowering the temperature of the reaction mixture below the gelling point of the gellable hydrocolloid. This well-recognized principle is illustrated in U.S. Pat. No. 2,800,457, where the process of a complex coacervation is disclosed in detail.
- the mixture may thus be made by forming an aqueous sol of one colloid, emulsifying the selected oil therein, and mixing the emulsion with an aqueous sol of another colloid, or the two sols may be made and mixed and the oil emulsified therein. [ . . . ]
- the process steps, down to the gelation step, are carried out with the ingredients at a temperature above the gel point of the colloid materials used, and gelation is brought about by cooling.
- GB 920,868 and WO 2004/022220 A1 both disclose forming the emulsions, which include the hydrophobic material to be encapsulated, at a temperature above the gel point.
- a further objective of the present invention relates to the wall-hardening step.
- Transglutaminase is an enzyme having its temperature optimum in the range of 45-55° C. and its pH optimum at about 6-7.
- U.S. Pat. No. 6,475,542 B1 and U.S. Pat. No. 6,592,916 B2 disclose simple coacervation processes, in which the cross-linking step is started at 30° C. but then conducted at an elevated temperature of 40° C., being closer to the temperature optimum of the enzyme. In these references it is mentioned that the enzyme reaction is usually carried out at 10 to 60° C.
- thermosenor 355 A2 a complex coacervation process with cross-linking by transglutaminase is disclosed.
- temperature during cross-linking in complex coacervation may be adjusted to 20° C. to 27° C. or to 5 to 10° C., but preferably the latter.
- pH is preferably adjusted to the optimum pH, that is, 7.
- cross-linking is carried out at very low temperatures, preferably about 5° C.
- Flavours and fragrances frequently fall in this category.
- bioactive principles such as flavours, fragrances, drugs, for example, encompass heat sensitive compounds. For avoiding degradation of such compounds, low temperature encapsulation processes would provide an additional advantage.
- the present invention has the objective of providing micro-capsules fulfilling worldwide religious and/or nutritional requirements.
- the present invention has the objective of using hydrocolloids and in particular gelatine that is kosher and/or halal.
- WO 96/20612 features the use of warm water fish gelatine in coacervation processes. Accordingly, it is taught that microencapsulation by complex coacervation has to be conducted at elevated temperatures, notably at temperatures of about 33-35° C. While the step of “microencapsulating” in this reference probably refers to the step of wall formation, it again becomes an objective of the present invention to manufacture micro-capsules at lower temperatures and hence, in a more economical way. It is in general an objective of the present invention to use warm water fish gelatine in a coacervation process, because it has been shown to provide capsule-walls having good heat-resistance and physical stability against shear forces. Furthermore, fish gelatine, while being kosher, is susceptible of obtaining halal status.
- the present inventors found that in coacervation processes, the step of adding a hydrophobic material to a hydrocolloid solution may be conducted at temperatures below the gelling temperature of a coacervate phase, the latter generally comprising gelatine.
- a coacervate phase the latter generally comprising gelatine.
- the formation of the wall of microcapsules obtained by coacervation can be initiated below the gelling temperature of the gelatine-based coacervate phase.
- the present invention provides a method of micro-encapsulating a hydrophobic material by coacervation, the method comprising the steps of:
- the present invention provides a method of preparing microcapsules by complex coacervation, the method comprising the step of cross-linking a hydrocolloid wall of the microcapsules with transglutaminase at a temperature in the range of 13-25° C. and at a pH in the range of 4-6.5.
- the present invention provides a method of preparing microcapsules by complex coacervation, the method comprising the step of cross-linking a hydrocolloid wall comprising warm water fish gelatine with transglutaminase, at a temperature in the range of 13-25° C.
- the method allows for conducting those steps involving the optionally volatile and/or thermal sensitive hydrophobic material at relatively low temperatures, while other steps, such as dissolving hydrocolloids, may still be conducted at elevated temperatures.
- the step of cross-linking may be conducted at about the pH adjusted for phase separation. Accordingly, repetitive adjustment of pH to the optimum of the respective step can be reduced.
- the present invention provides the use of warm water fish gelatine and cross-linking by transglutaminase, which entails advantages in terms of safety in general as well as in halal and kosher status.
- FIG. 1 shows the evolution of temperature and stirring speed as well as major process steps in the course of the method according to the present invention.
- Step A is the preparation of a diluted solution of gum Arabic and gelatine
- B represents a fast cooling step
- C refers to the introduction of the oily phase
- the temperature is kept at 25° C.
- step E cooling to the final temperature occurs.
- FIG. 2 is a microscopic view of the microcapsules obtained in Example 2.
- FIG. 3 is a microscopic view of the microcapsules obtained in Example 3.
- a hydrophobic material for the purpose of the present invention, may be in the liquid or solid state during the method of the invention. Preferably, it is liquid. Hydrophobic materials are generally regarded as materials that are not miscible in water at 25° C. and, when added to it, form a separate, hydrophobic phase.
- the term hydrophobic material includes material that is in the solid state at the temperatures generally employed in coacervation processes, that is, at less than or equal to about 50° C. Such solid material may be present in the form of crystals, for example. Preferably, if the solid material is liquefied by heating above its melting point, it forms a separate phase in water at that temperature.
- the hydrophobic material comprises flavours, fragrances, fats, oils, mouth-feel enhancers, neutraceuticals, drugs, other bioactive ingredients or mixtures thereof.
- flavour and fragrance materials are deemed to define a variety of flavour and fragrance materials of both natural and synthetic origins. They include single compounds or mixtures. Specific examples of such components may be found in the literature, e.g. in Fenaroli's Handbook of Flavor Ingredients, 1975, CRC Press; synthetic Food Adjuncts, 1947 by M. B. Jacobs, edited by van Nostrand; or Perfume and Flavor Chemicals by S. Arctander 1969, Montclair, N.J. (USA). These substances are well known to the person skilled in the art of perfuming, flavouring and/or aromatising consumer products, i.e. of imparting an odour and/or flavour or taste to a consumer product traditionally perfumed or flavoured, or of modifying the odour and/or taste of the consumer product.
- Neutraceuticals are edible materials such as foods or food ingredients that provide medical or health benefit to a human or animal individual upon consumption.
- Neutraceuticals include, for example, polyunsaturated fatty acids and/or oils comprising them, vitamins, minerals, co-enzyme Q, carnitine, botanical extracts, for example from gingseng, ginko biloba, Saint John's Wort, Saw Palmetto, functional foods such as oat, bran, psyllium, lignins, prebiotics, canola oil and stanols, for example.
- the hydrophobic material comprises flavours and/or fragrances.
- Many bioactive principles, but in particular flavours and/or fragrances, or compositions of flavours and/or fragrances have a high proportion of volatile compounds and/or components.
- the ingredient comprises at least 5 wt. %, preferably at least 10 wt. %, preferably at least 20 wt. %, more preferably at least 30 wt. % and most preferably at least 40 wt. % of chemical compounds having a vapour pressure of ⁇ 0.007 Pa at 25° C.
- At least 10 wt. % have a vapour pressure of ⁇ 0.1, more preferably, at least 10 wt. % have a vapour pressure of ⁇ 1 Pa at 25° C., and most preferably, at least 10 wt. % have a vapour pressure of ⁇ 10 Pa at 25° C.
- the value of 0.007 Pa at 25° C. is selected because it encompasses most of the compounds used by the skilled flavourist and/or perfumer. Compounds meeting these criteria are generally regarded as having a volatile character. In addition, compounds that remain odourless due to a lower volatility are excluded. The limit of 10 wt % of such compounds is regarded to constitute a substantial part of the ingredient.
- the method of the present invention allows for efficient encapsulation of more volatile ingredients being present in higher amounts of the total ingredients.
- the vapour pressure is determined by calculation. Accordingly, the method disclosed in “EPI suite”; 2000 U.S. Environmental Protection Agency, is used to determine the concrete value of the vapour pressure of a specific compound or component of the ingredient. This software is freely available and is based on average values of vapour pressures obtained by various methods of different scientists.
- the fragrance compound limonene is adduced for illustrating the determination of vapour pressure by calculation: by applying the method “EPI suite”, limonene is calculated to have a vapour pressure of about 193 Pa at 25° C.
- One of the methods of the present invention comprises the step of preparing a hydrocolloid solution by dissolving at least one protein and, optionally, a non-protein polymer in water.
- the non-protein polymer is charged oppositely to the protein.
- the present invention encompasses “simple” and “complex” coacervation.
- simple coacervation protein alone is used to form a capsule wall as phase separation is taking place.
- Complex coacervation refers to methods in which a generally oppositely charged non-protein polymer and a protein polymer together form the capsule wall.
- the present invention method provides the optional addition of an oppositely charged non-protein polymer, preferably a polysaccharide, to the hydrocolloid solution.
- colloids generally refers to hydrocolloids, that is polymeric substances that can be dissolved in water, optionally at elevated temperatures up to 90° C., for example. These encompass polymers such as proteins, polysaccharides and polyacids, for example, that are generally known to be useful in coacervation methods.
- Typical non-protein polymers useful in complex coacervation methods include, in particular, negatively charged polymers.
- they may be selected from gum arabic, xanthan, alginate salts, cellulose derivatives, for example carboxymethyl cellulose, pectinate salts, carrageenan, polyacrylic and methacrylic acid, and/or mixtures thereof.
- Further suitable non-proteins can be derived from the literature, for example from WO 2004/022221, page 4, lines 27-29.
- Proteins useful in coacervation processes include albumins, vegetable globulins and gelatines.
- the molecular weight of the protein is typically in the order of 40,000 to 500,000 preferably 20,000 to 250,000. Some protein aggregates, however, may have molecular weights in the millions.
- the protein is a gelatine. It is preferable to use gelatine having good physicochemical and chemical properties as typified by good film forming ability, amphoteric properties, the controllability of the quantity of charges by pH, and, preferably, the occurrence of the change from solution to gel at a critical temperature. Stated specifically, any gelatine that satisfies the specification for use in production of microcapsules may be employed.
- the gelatine may be fish, pork, beef, and/or poultry gelatine, for example.
- the protein is fish, beef or poultry gelatine.
- the protein is warm water fish gelatine.
- the warm water fish gelatine has a bloom of from about 150 to about 300 bloom, more preferably from about 200 to about 300 bloom.
- the warm water fish gelatine has ⁇ 250 bloom. According to the general knowledge, warm water fish are fish that are capable of tolerating water above 27° C. over prolonged time.
- the protein is halal. According to a further preferred embodiment the protein is kosher.
- the protein is present in an amount of from 0.5-3.5 wt %, preferably 1-2 wt. %.
- the polysaccharide is present in amounts of from 0.5-3.5 wt %, preferably 1-2% wt. % in the aqueous solution.
- concentrations may be obtained after an optional dilution step during which more concentrated stock-solutions are brought to concentrations useful for the steps of inducing the formation of the coacervate phase and/or forming capsule walls.
- An advantage of starting from more concentrated stock-solutions is that emulsion particle size can more easily be controlled in more concentrated hydrocolloid solutions.
- the methods of the present invention comprise a step of inducing the formation of a coacervate phase.
- the coacervate phase is generally based on the protein and, optionally, the non-polymer compound.
- This step is also referred to as phase separation.
- This step may be preferably accomplished by modifying, preferably lowering, the pH to or below the iso-electric point of the protein. If a non-protein polymer, for example a polysaccharide is present, the pH is preferably adjusted so that the positive charges on the proteins are neutralized by the negative charges on the non-protein polymer.
- Phase separation may be induced by various other ways, in general by changing the physico-chemical environment of the solution. Depending on the kind of coacervation process (simple; complex) different ways of inducing phase separation can be applied. For example, phase separation may be realized by salting out, by adding a second high molecular weight component so as to induce entropic phase separation of the wall material, for example.
- the methods of the present invention may comprise the step of cooling the hydrocolloid solution to a temperature below the gelling temperature of a coacervate phase based on the gelatine.
- the coacervate phase is free of a polysaccharide, whereas in complex coacervation processes the coacervate phase comprises the protein and at least one polysaccharide.
- the gelling temperature of the gellable protein used in the coacervation process of the present invention is considered to be equal to the gelling temperature of the coacervate phase of the present invention.
- the determination of the gelling temperature of the gellable protein, preferably gelatine needs to be established, in part by experiment.
- the gelling temperature corresponds to the critical temperature Tc described by Normand V. and Parker A. in “Scaling the Dynamics of Gelatin Gels”, 3 rd International symposium on Food Rheology and Structure, 2003, 185-189.
- Temperature Tc for any given gellable protein corresponds to the temperature at which the gel-forming dynamics exceed the gel-melting dynamics in a system.
- the critical temperature for any specific gellable protein is independent of concentration, despite of the impact of the latter on the kinetics of gel formation.
- the gelling temperature, Tc with an exactitude of ⁇ 1° C., is determined on the basis of equation 1 in Normand and Parker, 2003:
- Physica MCR 300 rheometer is employed (Anton Paar GmbH, Germany, www.anton-par.com), fitted with a 5 cm diameter, 2° angle cone and plate geometry. The gap is 50 ⁇ m. Oscillatory measurements are made at a frequency of 1 Hz and a constant 1% strain.
- G(t) measurements are made by oscillation as indicated above.
- the value obtained for G(t) characterises the mechanical resistance provided by a gel being formed.
- G(t) measurements are taken for a total of 20 hours, each minute in the first hour, every 10 minutes in the second hour, and once an hour from the beginning of the third hour.
- the critical temperature is the temperature Tc at which the best fit for the measured value is obtained, other parameters (Cc, ⁇ , ⁇ , ⁇ , ⁇ ) being constant.
- the best fit is represented by a master curve based on Equation 1, which corresponds to FIG. 2 of Normand and Parker (2003).
- the critical temperature is determined at a preciseness of ⁇ 1° C., as mentioned. Accordingly, from the above experimental setting in conjunction with Equation 1, the critical gelling temperature of a given gellable protein may be established. In accordance with a method of the present invention, the hydrocolloid solution comprising the gellable protein is cooled below this temperature, which is taken to be the gelling temperature of the coacervate phase.
- the gelling temperature of pork gelatine is generally in the range of 29° C.-36° C.
- the exact gelling temperature, however, of any gelatine selected from any pork, beef, poultry or warm water fish gelatine, for example, may be determined by the above methodology.
- the temperature of the solution is preferably reduced to or below these temperatures.
- this cooling step takes place before adding the hydrophobic material as detailed further below. Accordingly, the solution is cooled to 0-5° C., preferably 1-4° C., more preferably 2-3° C. below the gelling temperature of the gelatine used, before adding the hydrophobic material.
- the hydrophobic material is added to the solution with the solution having a temperature in the range of 22-33° C., preferably 24-32° C.
- the exact temperature will depend on the gelling temperature of the particular protein used, as indicated above on the example of gellable proteins such as gelatine.
- the methods of the present invention may comprise the step of preparing, after the cooling step, an emulsion and/or suspension by emulsifying and/or suspending a hydrophobic material in the solution.
- the cooling step prior to addition of adding the hydrophobic material by suspension or emulsion is performed comparatively quickly.
- this cooling step preferably takes place at about 1.4 to 4° C./min, preferably at 1.8 to 2.5° C./min.
- the emulsion and/or suspension may be prepared in a conventional manner.
- the hydrophobic material is slowly added during 3-10 min, preferably 4-6 min, with a stirrer being adjusted to 300-400 rpm.
- the size of emulsified droplets of hydrophobic material may be adjusted to an average diameter of 20-1000 ⁇ m, preferably 100-800, more preferably 150-700 ⁇ m, and most preferably of 250-350 ⁇ m. Average refers to the arithmetic mean.
- the diameter of the emulsified droplets or the suspended particles is taken as the size of the microcapsules of the present invention.
- the methods of the present invention may comprise a step of forming a colloid wall comprising the protein around droplets of the hydrophobic material present in an emulsion and/or suspension. This step takes place spontaneously once the step of formation of a coacervate phase is induced.
- the methods of the present invention preferably comprise a step of cross-linking the colloid wall.
- Cross-linking may be performed in any way, for example by adding sufficient amounts of formaldehyde and/or glutaraldehyde.
- cross-linking is effected enzymatically.
- cross-linking is effected with the enzyme Transglutaminase.
- transglutaminase is added at 10-100, preferably 30-60 activity units per gram of gelatine. This enzyme is well described and commercially obtainable.
- the temperature optimum of commercially available specimen of this enzyme is generally above 40° C. Accordingly, it is an advantage of the present invention that the cross-linking may be conducted at ambient temperatures, or, slightly cooled and/or heated temperatures, for example, relatively close to the temperature optimum of the enzyme.
- cross-linking in particular with transglutaminase, is conducted at a temperature in the range of 11-27° C.
- cross-linking may take place at a temperature in the range of 11-27° C., preferably 12-26° C., more preferably 13-25° C., even more preferably 14-24° C., e.g. 14-22° C.
- the pH during the cross-linking step is preferably adjusted to a level at which cross-linking can effectively be conducted.
- the pH may preferably be adjusted to 3-8, preferably 3.5-7.
- pH is adjusted to 3.5-6.5, preferably 4-6, most preferably 4-5.5.
- microcapsules produced by the methods of the present invention can be used in many kinds of applications or consumer end products, for example those in the fields of flavours and fragrances.
- they can be used for the flavouring of baking applications, meat, tobacco, frying and canning (thermal processing).
- flavouring of baking applications
- tobacco tobacco
- frying and canning thermo processing
- perfumery in the field of perfumery, they can be used for the perfuming of various consumer products such as household cleaners, pre-moistened wipes and personal care products. Therefore, perfuming or flavouring compositions comprising microcapsules according to the invention, optionally together with other perfuming or flavouring co-ingredients, are also aspects of the present invention.
- a stock solution of gelatine (solution A) is prepared by mixing 180 g of warm deionised water and 20 g of gelatine in a vessel until it is completely dissolved; the solution is then maintained at 40° C.
- a stock solution of gum Arabic (solution B) is prepared by mixing 180 g of cold deionised water and 20 g of gum Arabic in a vessel until it is completely dissolved; the solution is then warmed and kept at 40° C.
- the system is then diluted by the addition of 354.1 g of warm deionised water, which brings the total hydrocolloid concentration to 3.4% w/w.
- the mixture is finally cooled to 20° C. at a rate of 0.5° C./min.
- the stirring speed is slightly decreased, the pH is adjusted to 4.5 and 4.22 g of transglutaminase (ACTIVA® WM supplied by Ajinomoto, having 100 UA/g of enzyme) is added to the mixture.
- Cross-linking is allowed to proceed overnight at 20° C.
- a stock solution of gelatine (solution A) is prepared by mixing 180 g of warm deionised water and 20 g of gelatine in a vessel until it is completely dissolved; the solution is then maintained at 40° C.
- a stock solution of gum Arabic (solution B) is prepared by mixing 180 g of cold deionised water and 20 g of gum Arabic in a vessel until it is completely dissolved; the solution is then warmed and kept at 40° C.
- FIG. 1 The microcapsules thus obtained are shown in FIG. 1 .
- the microcapsules have an average diameter of 250 ⁇ m.
- FIG. 2 illustrates the evolution of the process in terms of temperature and stirring speed over time.
- Pork gelatine type A (275 Bloom) having a gelling temperature above 32° C., establish according to the methodology given in the description, and gum Arabic (Efficacia®, from CNI) are used as the hydrocolloids.
- a stock solution of gelatine (solution A) is prepared by mixing 180 g of warm deionised water and 20 g of gelatine in a vessel until it is completely dissolved; the solution is then maintained at 40° C.
- a stock solution of gum Arabic (solution B) is prepared by mixing 180 g of cold deionised water and 20 g of gum Arabic in a vessel until it is completely dissolved; the solution is then warmed and kept at 40° C.
- the microcapsules thus obtained are shown in FIG. 3 .
- the microcapsules have an average diameter of 250 ⁇ m.
- a stock solution of gelatine (solution A) is prepared by mixing 180 g of warm deionised water and 20 g of gelatine in a vessel until it is completely dissolved; the solution is then maintained at 40° C.
- a stock solution of gum Arabic (solution B) is prepared by mixing 180 g of cold deionised water and 20 g of gum Arabic in a vessel until it is completely dissolved; the solution is then warmed and kept at 40° C.
- microcapsules have an average diameter of 250 ⁇ m.
- Poultry gelatine 200 Bloom having a gelling temperature above 32°, as determined by the methodology provided in the description, and gum Arabic (Efficacia®, from CNI) are used as the hydrocolloids.
- a stock solution of gelatine (solution A) is prepared by mixing 180 g of warm deionised water and 20 g of gelatine in a vessel until it is completely dissolved; the solution is then maintained at 40° C.
- a stock solution of gum Arabic (solution B) is prepared by mixing 180 g of cold deionised water and 20 g of gum Arabic in a vessel until it is completely dissolved; the solution is then warmed and kept at 40° C.
- microcapsules have an average diameter of 250 ⁇ m.
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Abstract
Description
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- preparing a hydrocolloid solution by dissolving at least one protein and, optionally, a non-protein polymer, in water;
- cooling the hydrocolloid solution to a temperature below the gelling temperature of a coacervate phase based on the protein;
- preparing, after the cooling step, an emulsion and/or suspension by emulsifying and/or suspending a hydrophobic material in the solution;
- forming a colloid wall comprising protein around droplets and/or particles of the hydrophobic material present in an emulsion and/or suspension; and,
- cross-linking the colloid wall.
in which ε is the reduced temperature, ε=1−T/Tc in ° C., C is the concentration expressed as weight fraction, t is time and g(x) is a scaling function defining the shape of the master-curve according to Normand and Parker (2003). The four exponents and the critical concentration, Cc, are fitting parameters. For the purpose of the present invention, the exponents are considered to be constants, that is, α=3.2, β=−9.3, μ=2.3 and ν=−2.6. Cc is considered to be 0. These values are used as approximate simplification but are generally found to match the situation encountered with most gelatines.
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PCT/IB2007/050899 WO2007113706A1 (en) | 2006-04-04 | 2007-03-15 | Method for preparing microcapsules by coacervation |
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GB202018995D0 (en) | 2020-12-02 | 2021-01-13 | Givaudan Sa | Improvements in or relating to organic compounds |
WO2022112204A1 (en) | 2020-11-25 | 2022-06-02 | Givaudan Sa | Improvements in or relating to organic compounds |
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- 2007-03-15 BR BRPI0710224A patent/BRPI0710224B1/en active IP Right Grant
- 2007-03-15 WO PCT/IB2007/050899 patent/WO2007113706A1/en active Application Filing
- 2007-03-15 JP JP2009503699A patent/JP4829341B2/en active Active
- 2007-03-15 AT AT07735133T patent/ATE510615T1/en not_active IP Right Cessation
- 2007-03-15 MX MX2008012564A patent/MX2008012564A/en active IP Right Grant
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US10561621B2 (en) | 2010-09-20 | 2020-02-18 | Diane Goll | Microencapsulation process and product |
US11723877B2 (en) | 2010-09-20 | 2023-08-15 | Spi Pharma, Inc. | Microencapsulation process and product |
WO2022112204A1 (en) | 2020-11-25 | 2022-06-02 | Givaudan Sa | Improvements in or relating to organic compounds |
GB202018995D0 (en) | 2020-12-02 | 2021-01-13 | Givaudan Sa | Improvements in or relating to organic compounds |
Also Published As
Publication number | Publication date |
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JP4829341B2 (en) | 2011-12-07 |
CN101410175A (en) | 2009-04-15 |
ES2365076T3 (en) | 2011-09-21 |
WO2007113706A1 (en) | 2007-10-11 |
BRPI0710224A2 (en) | 2011-08-02 |
EP2004321A1 (en) | 2008-12-24 |
BRPI0710224B1 (en) | 2016-07-26 |
EP2004321B1 (en) | 2011-05-25 |
JP2009532202A (en) | 2009-09-10 |
ATE510615T1 (en) | 2011-06-15 |
US20090253165A1 (en) | 2009-10-08 |
CN101410175B (en) | 2013-11-20 |
MX2008012564A (en) | 2008-10-10 |
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